WO1991014783A1 - A process for decomposing peroxycarboxylic acids - Google Patents
A process for decomposing peroxycarboxylic acids Download PDFInfo
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- WO1991014783A1 WO1991014783A1 PCT/DK1991/000084 DK9100084W WO9114783A1 WO 1991014783 A1 WO1991014783 A1 WO 1991014783A1 DK 9100084 W DK9100084 W DK 9100084W WO 9114783 A1 WO9114783 A1 WO 9114783A1
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- peroxycarboxylic
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids
Definitions
- the present invention relates to a process for decomposing peroxycarboxylic acids by treatment with a catalyst.
- Peroxycarboxylic acids constitute an important class of sub ⁇ stances which may be used for a wide range of purposes.
- peroxycarboxylic acids are commonly employed as oxidizing reagents in the field of organic synthesis for the production of a variety of organic chemicals.
- organic molecules containing unsaturations or other reducing groups may be oxidized in a high yield under mild conditions when subjected to peroxycarboxylic acids during organic synthesis, and consequently peroxycarboxylic acids may advantageously be used, e.g., for the preparation of epoxides from unsaturated hydrocarbons.
- peroxycarboxylic acids may also be used as bleaching agents, for instance to decolourize paper mill process streams.
- Fur ⁇ thermore preparations of peroxycarboxylic acids may be used for disinfection purposes (e.g. in the food industry) due to the sensitivity of microorganisms to these compounds (see e.g. H.C. Flemming, Zbl.Ba t.Hyg. , I.Abt.Orig. B 179, 97-111 (1984)) .
- peroxycarboxylic acids are highly advantageous reagents for these and other applications, their continued presence in the end products is not always desirable as they represent a potential environmental or health hazard.
- solu ⁇ tions of dyes decolourized by means of peroxycarboxylic acids should preferably be free from remaining peroxycarboxylic acid before being discharged into the environment where the peroxycarboxylic acid might exert a harmful effect.
- utensils and surfaces disinfected in the food industry by means of peroxycarboxylic acids should be free from the reagent prior to use since the peroxycarboxylic acid may otherwise deteriorate the food product produced or eventually reach the consumer.
- substances prepared by chemical synthesis utilizing peroxycarboxylic acids should be free from the oxidation reagent which for instance might un ⁇ desirably influence the further use or conversion of the syn ⁇ thesized substance.
- the present invention relates to a process for converting peroxycarboxylic acids to carboxylic acids, the process comprising treating a peroxycarboxylic acid of the general formula I:
- R is a linear or branched alkyl group, an aryl group or an aryl-alkyl group each of which may optionally be sub ⁇ stituted with one or more hydroxy, halogen, alkoxy, amino, alkylamino, sulfoxy, sulfono, amido, carboxy, percarboxy or nitro groups, with an enzyme catalyst to form the correspond ⁇ ing carboxylic acid of the general formula II:
- German Patent 2 240 605 Cold- Palmolive Co.
- hydrolases in particular esterases or lipases of plant or animal origin, for generat ⁇ ing peroxycarboxylic acids from simple ester substrates.
- lipases in general and a lipase derived from Pseudomonas pu ida in particular for generating peroxy ⁇ carboxylic acids from ester substrates is described in EP 253 487 and EP 268 456 (both to Clorox) .
- a similar use of pro ⁇ teases is described in EP 310 952 (Henkel) . To the best of the present inventors' knowledge, however, it has not pre ⁇ viously been proposed to degrade peroxycarboxylic acids by means of such enzymes.
- Enzymes which may be employed as catalysts in the process of the invention are preferably hydrolases such as proteases, esterases and lipases. From the point of view of cost and availability it is advantageous to employ enzymes producible by microorganisms such as yeasts, bacteria or fungi.
- Lipases which may be employed in the present process may be microbial lipases produced, for instance, by strains of As- per ⁇ illus- Enterobacterium. Chromobacteriu - Geotricium or Penicillium.
- Preferred lipases for use according to the in- vention are those produced by species of Asperqillus, Mucor, Humicola, Pseudomonas or Candida.
- Particularly preferred lipases are those produced by the fol ⁇ lowing strains of microorganisms:
- the strain producing the enzyme may be cultivated under aerobic conditions in a nutrient medium con- taining assimilable carbon and nitrogen sources as well as essential minerals, trace elements etc. , the medium being composed according to established practice.
- liquid enzyme concentrates may be prepared by removing insoluble materials, e.g. by filtration or centrifugation, after which the culture broth may be concentrated by evapora ⁇ tion or reverse osmosis.
- Solid enzyme preparations may be prepared from the concentrate by precipitation with salts or water-miscible solvents, e.g. ethanol, or by drying such as spray-drying in accordance with well-known methods.
- lipases which may be used in the process of the inven ⁇ tion are commercial lipases, e.g., those known under the trade names Palatase ® (a lipase obtainable from Aspercrillus niger, available from Novo Nordisk A/S) and LipolaseTM (also obtainable from Novo Nordisk A/S) .
- Palatase ® a lipase obtainable from Aspercrillus niger, available from Novo Nordisk A/S
- LipolaseTM also obtainable from Novo Nordisk A/S
- the lipase may furthermore be one producible by recombinant DNA techniques, cf. for instance EP 238 023.
- the esterase employed in the process of the invention may be of animal or microbial origin.
- a suitable esterase for the present purpose is one obtainable from hog liver.
- the enzyme When employed in the process of the invention, the enzyme may be in a soluble state. It is, however, preferred to immo ⁇ bilize the enzyme on a solid support in order to facilitate the separation of the enzyme from the material treated with peroxycarboxylic acid. Immobilization procedures are well known (cf. for instance K. Mosbach, ed. , "Immobilized En- zy es", Methods in Enzymology 44, Academic Press, New York, 1976) and include cross-linking of cell homogenates, covalent coupling to insoluble organic or inorganic supports, entrap ⁇ ment in gels and adsorption to ion exchange resins or other adsorbent materials. Coating on a particulate support may also be employed (cf.
- Suitable support materials for the immobilized en ⁇ zyme are, for instance, plastics (e.g. polypropylene, poly ⁇ styrene, polyvinylchloride, polyurethane, latex, nylon, poly- tetrafluoroethylene, polyethylene terephthalates, polyvinyl- acetate, polyvinylalcohol or any suitable copolymer thereof) , polysaccharides (e.g. agarose or dextran) , ion exchange resins (both cation and anion exchange resins) , silicon poly ⁇ mers (e.g. siloxane) or silicates (e.g. glass) .
- plastics e.g. polypropylene, poly ⁇ styrene, polyvinylchloride, polyurethane, latex, nylon, poly- tetrafluoroethylene, polyethylene terephthalates, polyvinyl- acetate, polyvinylalcohol or any suitable copo
- a particularly preferred resin is a weakly basic anion exchange resin which may be a polystyrene-, acrylic- or phenol-formaldehyde-type resin.
- Examples of commercially available resins are Lewatit E 1999/85 or E2001/85 (registered trademark of Bayer, Federal Republic of Germany) and Duolite ES-568 (registered trademark of Rohm & Haas, FRG) .
- Immobilization of enzymes to acrylic- type resins may be carried out according to EP 140 542.
- Immo- bilization to phenol-formaldehyde-type resins may be done according to DK 85/878.
- Another convenient material for immobilizing enzymes is an inorganic support, such as a silicate.
- the enzyme may be attached to the support by adsorption or by covalent coupl ⁇ ing, e.g. as described in K. Mosbach, ed. , op. cit.
- R in the general formulae I and II above is preferably a linear alkyl group, in particular a linear alkyl group with 1-19 carbon atoms, preferably 1-13 carbon atoms, more prefer- ably 1-10 carbon atoms and most preferably 2 or 8-10 carbon atoms.
- R may also be an alkyl group substituted by one or more halogen atoms, preferably chloro atoms.
- the conversion of the peroxy ⁇ carboxylic acid (I) to the carboxylic acid (II) may be carried out in an aqueous medium.
- an aqueous solution such as a solution of pigments or a solution of peroxycar ⁇ boxylic acid used for disinfection purposes.
- the process of the invention is particularly useful in con ⁇ nection with bleaching processes, disinfection processes and organic synthesis processes involving the use of peroxycar ⁇ boxylic acids.
- any peroxycarboxylic acid remaining after the oxidation process may conveniently be re- moved by treatment with the enzyme catalyst. Since enzymes exhibit a high affinity for their substrates (in this case the peroxycarboxylic acids) and a high degree of specificity, the conversion of the peroxycarboxylic acid may be carried out substantially without affecting any other compounds present, and may furthermore be used to remove even small amounts of peroxycarboxylic acid.
- the process of the present invention may suitab ⁇ ly be employed for the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) in a step subsequent to disinfecting an object (e.g. a utensil or a surface) with the peroxycarboxylic acid (I) .
- the process of the invention may be em ⁇ ployed for the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) in a subsequent step to bleaching a coloured substance with the peroxycar- boxylic acid (I) .
- the process of the invention may be employed for the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) in a subsequent step to the oxidation of organic or inorganic substrates with a peroxycarboxylic acid (I).
- suitable hydrogen peroxide converting enzymes are catalase, peroxidases, and haloperoxidases.
- Peroxycarboxylic acids were prepared according to the method described by W. E. Parker, C. Ricciuti, C. L. Ogg and D. Swern, J. Am. Chem. Soc. 77, 4037 (1955) except for peracetic acid which was obtained as an approximately 2 M solution under the trademark Proxitane 507.
- Peroxycarboxylic acid levels may be determined, also when hydrogen peroxide is present together with the peroxycarboxylic acid, by methods known in the art, e.g. by iodometry at 5°C as described by Sully and Williams in Analyst. 1962, 87, 653 (this method also gives the concentration of hydrogen peroxide) .
- One Lipase Unit is the amount of enzyme which liberates one micromole of butyric acid per minute from tributyrin as a substrate in a pH-stat at 30°C and pH 7 (a detailed descrip ⁇ tion of the assay (AF 95) is available from Novo Nordisk A/S upon request) .
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Abstract
The invention relates to a process for converting peroxycarboxylic acids to carboxylic acids, the process comprising treating a peroxycarboxylic acid of the general formula: R-CO-OOH, wherein R is a linear or branched alkyl group, an aryl group or an aryl-alkyl group each of which may optionally be substituted with one or more hydroxy, halogen, alkoxy, amino, alkylamino, sulfo, sulfoxy, sulfono, amido, carboxy, percarboxy or nitro groups, with an enzyme catalyst to form the corresponding carboxylic acid of the general formula: R-CO-OH, wherein R has the meaning indicated above.
Description
A PROCESS FOR DECOMPOSING PEROXYCARBOXYLIC ACIDS
FIELD OF INVENTION
The present invention relates to a process for decomposing peroxycarboxylic acids by treatment with a catalyst.
BACKGROUND OF THE INVENTION
Peroxycarboxylic acids constitute an important class of sub¬ stances which may be used for a wide range of purposes. Thus, peroxycarboxylic acids are commonly employed as oxidizing reagents in the field of organic synthesis for the production of a variety of organic chemicals. In particular, organic molecules containing unsaturations or other reducing groups may be oxidized in a high yield under mild conditions when subjected to peroxycarboxylic acids during organic synthesis, and consequently peroxycarboxylic acids may advantageously be used, e.g., for the preparation of epoxides from unsaturated hydrocarbons. Apart from their use as oxidation reagents, peroxycarboxylic acids may also be used as bleaching agents, for instance to decolourize paper mill process streams. Fur¬ thermore, preparations of peroxycarboxylic acids may be used for disinfection purposes (e.g. in the food industry) due to the sensitivity of microorganisms to these compounds (see e.g. H.C. Flemming, Zbl.Ba t.Hyg. , I.Abt.Orig. B 179, 97-111 (1984)) .
While peroxycarboxylic acids are highly advantageous reagents for these and other applications, their continued presence in the end products is not always desirable as they represent a potential environmental or health hazard. For instance, solu¬ tions of dyes decolourized by means of peroxycarboxylic acids should preferably be free from remaining peroxycarboxylic acid before being discharged into the environment where the peroxycarboxylic acid might exert a harmful effect. Similar¬ ly, utensils and surfaces disinfected in the food industry by
means of peroxycarboxylic acids should be free from the reagent prior to use since the peroxycarboxylic acid may otherwise deteriorate the food product produced or eventually reach the consumer. Furthermore, substances prepared by chemical synthesis utilizing peroxycarboxylic acids should be free from the oxidation reagent which for instance might un¬ desirably influence the further use or conversion of the syn¬ thesized substance.
Accordingly, there is a need for processes whereby residual peroxycarboxylic acids may be removed, in particular pro¬ cesses which allow for selective decomposition of peroxy¬ carboxylic acids under mild conditions and which may thus be applied for the removal of peroxycarboxylic acids without adversely affecting other components in the peroxycarboxylic acid containing medium. Such processes should preferably also be economically viable for the treatment of large volumes of very dilute peroxycarboxylic acid containing solutions. To the present inventors' knowledge, no entirely satisfactory processes for the removal of peroxycarboxylic acids are currently available, and the use of peroxycarboxylic acids is accordingly limited, no matter how desirable their applica¬ tion in many processes may be.
SUMMARY OF THE INVENTION
It has surprisingly been found that certain enzymes may ad- vantageously be used for the conversion of peroxycarboxylic acids to the corresponding carboxylic acids. Such enzymatic processes permit selective transformation of peroxycarboxylic acids under mild conditions and provide an economical way of removing peroxycarboxylic acids from large volumes of dilute solutions of the peroxycarboxylic acids.
Accordingly, the present invention relates to a process for converting peroxycarboxylic acids to carboxylic acids, the
process comprising treating a peroxycarboxylic acid of the general formula I:
R-CO-OOH (I)
wherein R is a linear or branched alkyl group, an aryl group or an aryl-alkyl group each of which may optionally be sub¬ stituted with one or more hydroxy, halogen, alkoxy, amino, alkylamino, sulfoxy, sulfono, amido, carboxy, percarboxy or nitro groups, with an enzyme catalyst to form the correspond¬ ing carboxylic acid of the general formula II:
R-CO-OH (II)
The use of enzymes (especially hydrolases) has previously been proposed for the formation of peroxycarboxylic acids in aqueous solutions. Thus German Patent 2 240 605 (Colgate- Palmolive Co.) suggests the use of hydrolases, in particular esterases or lipases of plant or animal origin, for generat¬ ing peroxycarboxylic acids from simple ester substrates. Likewise the use of lipases in general and a lipase derived from Pseudomonas pu ida in particular for generating peroxy¬ carboxylic acids from ester substrates is described in EP 253 487 and EP 268 456 (both to Clorox) . A similar use of pro¬ teases is described in EP 310 952 (Henkel) . To the best of the present inventors' knowledge, however, it has not pre¬ viously been proposed to degrade peroxycarboxylic acids by means of such enzymes.
DETAILED DESCRIPTION OF THE INVENTION
Enzymes which may be employed as catalysts in the process of the invention are preferably hydrolases such as proteases, esterases and lipases. From the point of view of cost and availability it is advantageous to employ enzymes producible by microorganisms such as yeasts, bacteria or fungi.
Lipases which may be employed in the present process may be microbial lipases produced, for instance, by strains of As- perσillus- Enterobacterium. Chromobacteriu - Geotricium or Penicillium. Preferred lipases for use according to the in- vention are those produced by species of Asperqillus, Mucor, Humicola, Pseudomonas or Candida.
Particularly preferred lipases are those produced by the fol¬ lowing strains of microorganisms:
Humicola lanuqinosa. DSM 3819 and 4109, Humicola brevispora, DSM 4110,
Humicola brevis var. thermoidea. DSM 4111, and
Humicola insolens, DSM 1800.
To produce the lipase, the strain producing the enzyme may be cultivated under aerobic conditions in a nutrient medium con- taining assimilable carbon and nitrogen sources as well as essential minerals, trace elements etc. , the medium being composed according to established practice. After cultiva¬ tion, liquid enzyme concentrates may be prepared by removing insoluble materials, e.g. by filtration or centrifugation, after which the culture broth may be concentrated by evapora¬ tion or reverse osmosis. Solid enzyme preparations may be prepared from the concentrate by precipitation with salts or water-miscible solvents, e.g. ethanol, or by drying such as spray-drying in accordance with well-known methods.
Other lipases which may be used in the process of the inven¬ tion are commercial lipases, e.g., those known under the trade names Palatase® (a lipase obtainable from Aspercrillus niger, available from Novo Nordisk A/S) and Lipolase™ (also obtainable from Novo Nordisk A/S) .
The lipase may furthermore be one producible by recombinant DNA techniques, cf. for instance EP 238 023.
The esterase employed in the process of the invention may be of animal or microbial origin. A suitable esterase for the present purpose is one obtainable from hog liver.
When employed in the process of the invention, the enzyme may be in a soluble state. It is, however, preferred to immo¬ bilize the enzyme on a solid support in order to facilitate the separation of the enzyme from the material treated with peroxycarboxylic acid. Immobilization procedures are well known (cf. for instance K. Mosbach, ed. , "Immobilized En- zy es", Methods in Enzymology 44, Academic Press, New York, 1976) and include cross-linking of cell homogenates, covalent coupling to insoluble organic or inorganic supports, entrap¬ ment in gels and adsorption to ion exchange resins or other adsorbent materials. Coating on a particulate support may also be employed (cf. for instance A.R. Macrae and R.C. Ham¬ mond, Biotechnology and Genetic Engineering Reviews 3, 1985, p. 193) . Suitable support materials for the immobilized en¬ zyme are, for instance, plastics (e.g. polypropylene, poly¬ styrene, polyvinylchloride, polyurethane, latex, nylon, poly- tetrafluoroethylene, polyethylene terephthalates, polyvinyl- acetate, polyvinylalcohol or any suitable copolymer thereof) , polysaccharides (e.g. agarose or dextran) , ion exchange resins (both cation and anion exchange resins) , silicon poly¬ mers (e.g. siloxane) or silicates (e.g. glass) .
It is preferred to immobilize the enzyme on an ion exchange resin by adsorbing the enzyme to the resin or by cross-link¬ ing it to the resin by means of glutaraldehyde or another cross-linking agent in a manner known per se. A particularly preferred resin is a weakly basic anion exchange resin which may be a polystyrene-, acrylic- or phenol-formaldehyde-type resin. Examples of commercially available resins are Lewatit E 1999/85 or E2001/85 (registered trademark of Bayer, Federal Republic of Germany) and Duolite ES-568 (registered trademark of Rohm & Haas, FRG) . Immobilization of enzymes to acrylic- type resins may be carried out according to EP 140 542. Immo-
bilization to phenol-formaldehyde-type resins may be done according to DK 85/878.
Another convenient material for immobilizing enzymes is an inorganic support, such as a silicate. The enzyme may be attached to the support by adsorption or by covalent coupl¬ ing, e.g. as described in K. Mosbach, ed. , op. cit.
R in the general formulae I and II above is preferably a linear alkyl group, in particular a linear alkyl group with 1-19 carbon atoms, preferably 1-13 carbon atoms, more prefer- ably 1-10 carbon atoms and most preferably 2 or 8-10 carbon atoms. R may also be an alkyl group substituted by one or more halogen atoms, preferably chloro atoms.
According to the invention, the conversion of the peroxy¬ carboxylic acid (I) to the carboxylic acid (II) may be carried out in an aqueous medium. This is an advantage when the peroxycarboxylic acid treatment preceding the present process takes place in, for instance, an aqueous solution, such as a solution of pigments or a solution of peroxycar¬ boxylic acid used for disinfection purposes.
The process of the invention is particularly useful in con¬ nection with bleaching processes, disinfection processes and organic synthesis processes involving the use of peroxycar¬ boxylic acids. In these instances any peroxycarboxylic acid remaining after the oxidation process may conveniently be re- moved by treatment with the enzyme catalyst. Since enzymes exhibit a high affinity for their substrates (in this case the peroxycarboxylic acids) and a high degree of specificity, the conversion of the peroxycarboxylic acid may be carried out substantially without affecting any other compounds present, and may furthermore be used to remove even small amounts of peroxycarboxylic acid.
Accordingly, the process of the present invention may suitab¬ ly be employed for the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) in a step subsequent to disinfecting an object (e.g. a utensil or a surface) with the peroxycarboxylic acid (I) . In another favoured embodiment, the process of the invention may be em¬ ployed for the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) in a subsequent step to bleaching a coloured substance with the peroxycar- boxylic acid (I) . In yet another favoured embodiment, the process of the invention may be employed for the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) in a subsequent step to the oxidation of organic or inorganic substrates with a peroxycarboxylic acid (I).
Certain enzymes, when employed according to the invention, will give rise to the formation of hydrogen peroxide con- comitantly with conversion of the peroxycarboxylic acid as shown in Reaction Scheme 1 below in which R has the meaning indicated above:
Reaction Scheme 1:
Enzyme R-CO-OOH > R-CO-OH + H202
(I) (II)
In some cases, it may be advantageous to convert the hydrogen peroxide formed in the reaction with an enzyme with a view to removing this oxidizing species from the reaction mixture or initiating oxidizing processes in the reaction medium, based on the use of hydrogen peroxide. Accordingly, it may be ad- vantageous to carry out the conversion of the peroxycar¬ boxylic acid (I) in the presence of a hydrogen peroxide con¬ verting enzyme or, alternatively, to subject the hydrogen
peroxide formed as a result of the conversion of the peroxy¬ carboxylic acid (I) to subsequent treatment with a hydrogen peroxide converting enzyme. Examples of suitable hydrogen peroxide converting enzymes are catalase, peroxidases, and haloperoxidases.
The process of the invention is further illustrated by the following examples which are not intended to be in any way limiting to the scope of the invention as claimed.
EXAMPLES
General Methods
Peroxycarboxylic acids were prepared according to the method described by W. E. Parker, C. Ricciuti, C. L. Ogg and D. Swern, J. Am. Chem. Soc. 77, 4037 (1955) except for peracetic acid which was obtained as an approximately 2 M solution under the trademark Proxitane 507. Peroxycarboxylic acid levels may be determined, also when hydrogen peroxide is present together with the peroxycarboxylic acid, by methods known in the art, e.g. by iodometry at 5°C as described by Sully and Williams in Analyst. 1962, 87, 653 (this method also gives the concentration of hydrogen peroxide) . One Lipase Unit (LU) is the amount of enzyme which liberates one micromole of butyric acid per minute from tributyrin as a substrate in a pH-stat at 30°C and pH 7 (a detailed descrip¬ tion of the assay (AF 95) is available from Novo Nordisk A/S upon request) .
Example 1.
To a 0.47 mM solution of peroctanoic acid in a 50 M phos¬ phate buffer at pH 7 and 40°C was added 10 LU/ml PalataseR (a fungal lipase produced by fermentation of a strain of Asper- gillus niger) , and the peroxycarboxylic acid concentration was monitored as a function of time (the numbers in brackets
refer to a reference-experiment performed under similar con¬ ditions but without addition of enzyme) :
) Not detectable.
Example 2
To a 0.56 mM solution of peracetic acid in a 50 mM phosphate buffer at pH 7 and 40°C was added 10 LU/ml PalataseR (as de¬ scribed in example 1) and the peroxycarboxylic acid concen¬ tration was monitored as a function of time :
Time after addition Peracid concentration (mM) of enzyme (min) 0 0.56
4 0.26
9 0.08
14 0 (not detectable)
In a similar experiment, but without any addition of enzyme, the peroxycarboxylic acid concentration declined much more slowly as shown in the following table :
Time (min) Peracid concentration (mM)
0 0.61
5 0.57 10 0.55
15 0.53
Example 3
To a 0.2 mM solution of peracetic acid in a 50 mM phosphate buffer pH 8 and 25°C was added 50 U/ml (Sigma units) Esterase from Hog Liver (Sigma E-3128, 6365 U/ml) and the peroxycarboxylic acid concentration was monitored as a func¬ tion of time :
Time after addition Peracid concentration (mM) of enzyme (min)
0 0.20 2 0.15
10 0 (not detectable)
18 0 (not detectable)
In a corresponding experiment with no enzyme, the peracetic acid concentration did not change within 18 min.
Example 4
To a solution of 0.5 mM pernonanoic acid in 15 mM phosphate buffer at pH 8.5 and 22°C was added 5 LU/ml Lipolase™ (available from Novo Nordisk A/S) and both the peroxycarboxy- lie acid concentration and the concentration of H202 was monitored as a function of time:
Time Concentrations (mM) Pernonanoic acid H2°2
Immediately after addition of enzyme 0.30 0.08
13 min later 0.32
(not detectable)
In a corresponding experiment with no enzyme, the peroxycar- boxylic acid concentration was unchanged after 14 min.
Claims
1. A process for converting peroxycarboxylic acids to car¬ boxylic acids, the process comprising treating a peroxycar¬ boxylic acid of the general formula I:
R-CO-OOH (I)
wherein R is a linear or branched alkyl group, an aryl group or an aryl-alkyl group each of which may optionally be sub¬ stituted with one or more hydroxy, halogen, alkoxy, amino, alkylamino, sulfo, sulfoxy, sulfono, amido, carboxy, percar- boxy or nitro groups, with an enzyme catalyst to form the corresponding carboxylic acid of the general formula II:
R-CO-OH (II)
wherein R has the meaning indicated above.
2. A process according to claim 1, wherein the enzyme is a hydrolase, such as an esterase, protease or lipase.
3. A process according to claim 2, wherein the enzyme is a microbial lipase.
4. A process according to claim 3, wherein the lipase is one obtainable from a strain of Mucor, Aspergillus. Humicola. Pseudomonas or Candida.
5. A process according to any of claims 1-4, wherein the en¬ zyme is immobilized on a solid support.
6. A process according to any of claims 1-5, wherein R is a linear alkyl group, in particular a linear alkyl group with 1-19 carbon atoms, preferably with 1-13 carbon atoms, more preferably with 1-10 carbon atoms and most preferably with 2 or 8-10 carbon atoms.
7. A process according to any of claims 1-6, wherein R is an alkyl group substituted with one or more halogen atoms, preferably chlorine atoms.
8. A process according to any of claims 1-7, wherein the con- 5 version of the peroxycarboxylic acid (I) is carried out in an aqueous medium.
9. A process according to any of claims 1-8, wherein the con¬ version of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) is a subsequent step to disin-
10 fecting an object with the peroxycarboxylic acid (I) .
10. A process according to any of claims 1-8, wherein the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) is a subsequent step to bleaching a coloured substance with the peroxycarboxylic acid
15 (I).
11. A process according to any of claims 1-8, wherein the conversion of the peroxycarboxylic acid (I) or residues thereof to the carboxylic acid (II) is a subsequent step to the oxidation of organic or inorganic substrates with a per-
20 oxycarboxylic acid (I) .
12. A process according to any of the preceding claims, wherein the conversion of the peroxycarboxylic acid (I) is carried out in the presence of or followed by treatment with a hydrogen peroxide decomposing enzyme.
2513. A process according to claim 12, wherein the hydrogen peroxide decomposing enzyme is a catalase, a peroxidase or a haloperoxidase.
Priority Applications (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP91906505A EP0521951B1 (en) | 1990-03-20 | 1991-03-19 | A process for decomposing peroxycarboxylic acids |
| DE69103626T DE69103626T2 (en) | 1990-03-20 | 1991-03-19 | METHOD FOR DEGREASING PEROXIC CARBONIC ACIDS. |
| JP91506283A JPH05505723A (en) | 1990-03-20 | 1991-03-19 | Decomposition method of peroxycarboxylic acid |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK0714/90 | 1990-03-20 | ||
| DK071490A DK71490D0 (en) | 1990-03-20 | 1990-03-20 | A PROCEDURE FOR MAKING ORGANIC COMPOUNDS |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO1991014783A1 true WO1991014783A1 (en) | 1991-10-03 |
Family
ID=8096698
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/DK1991/000084 WO1991014783A1 (en) | 1990-03-20 | 1991-03-19 | A process for decomposing peroxycarboxylic acids |
Country Status (7)
| Country | Link |
|---|---|
| EP (1) | EP0521951B1 (en) |
| JP (1) | JPH05505723A (en) |
| AT (1) | ATE110416T1 (en) |
| DE (1) | DE69103626T2 (en) |
| DK (2) | DK71490D0 (en) |
| ES (1) | ES2060375T3 (en) |
| WO (1) | WO1991014783A1 (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5541092A (en) * | 1989-09-12 | 1996-07-30 | Novo Nordisk A/S | Process for preparing peroxycarboxylic acids using lipase in a non-aqueous medium |
| CN114591250A (en) * | 2022-03-19 | 2022-06-07 | 杭州布朗生物医药科技有限公司 | One-step synthesis method of 5-bromo-2-chloropyrimidine |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE102018113300A1 (en) * | 2018-06-05 | 2019-12-05 | Krones Ag | Method and measuring device for determining a peracetic acid concentration in a peracetic acid and hydrogen peroxide-containing sterilizing medium |
-
1990
- 1990-03-20 DK DK071490A patent/DK71490D0/en not_active Application Discontinuation
-
1991
- 1991-03-19 WO PCT/DK1991/000084 patent/WO1991014783A1/en active IP Right Grant
- 1991-03-19 ES ES91906505T patent/ES2060375T3/en not_active Expired - Lifetime
- 1991-03-19 DE DE69103626T patent/DE69103626T2/en not_active Expired - Fee Related
- 1991-03-19 JP JP91506283A patent/JPH05505723A/en active Pending
- 1991-03-19 EP EP91906505A patent/EP0521951B1/en not_active Expired - Lifetime
- 1991-03-19 DK DK91906505.2T patent/DK0521951T3/en active
- 1991-03-19 AT AT91906505T patent/ATE110416T1/en not_active IP Right Cessation
Non-Patent Citations (3)
| Title |
|---|
| CHEMICAL ABSTRACTS, Volume 82, No. 17, 28 April 1975, (Columbus, Ohio, US), PETER JONES et al. "Formation of catalase compound I by reaction with peroxoacetic acid. pH changes in unbuffered systems", see page 185, Abstract 108080h, & Biochem. J. 1974, 143(2), 473-474. * |
| CHEMICAL ABSTRACTS, Volume 93, No. 9, 1 September 1980, (Columbus, Ohio, US), MONICA M. PALCIC et al. "The reaction of human erythrocyte catalase with hydroperoxides to form compound I", see page 269, Abstract 91006r, & J. BIOL. CHEM. 1980, 255(13), 6128-6132. * |
| CHEMICAL ABSTRACTS, Volume 94, No. 25, 22 June 1981, (Columbus, Ohio, US), TSUNEHISA ARAISO et al. "Kinetic analysis of compound I formation and the catalatic activity of chloroperoxidase", see page 225, Abstract 204484m, & Can. J. Biochem. 1981, 59(4), 233-236. * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5541092A (en) * | 1989-09-12 | 1996-07-30 | Novo Nordisk A/S | Process for preparing peroxycarboxylic acids using lipase in a non-aqueous medium |
| CN114591250A (en) * | 2022-03-19 | 2022-06-07 | 杭州布朗生物医药科技有限公司 | One-step synthesis method of 5-bromo-2-chloropyrimidine |
Also Published As
| Publication number | Publication date |
|---|---|
| DK0521951T3 (en) | 1995-01-09 |
| ATE110416T1 (en) | 1994-09-15 |
| EP0521951B1 (en) | 1994-08-24 |
| EP0521951A1 (en) | 1993-01-13 |
| ES2060375T3 (en) | 1994-11-16 |
| JPH05505723A (en) | 1993-08-26 |
| DE69103626T2 (en) | 1995-01-19 |
| DK71490D0 (en) | 1990-03-20 |
| DE69103626D1 (en) | 1994-09-29 |
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